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Entry version 112 (25 May 2022)
Sequence version 1 (01 Nov 1996)
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Protein

Bifunctional abietadiene synthase, chloroplastic

Gene

AS

Organism
Abies grandis (Grand fir) (Pinus grandis)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Involved in defensive oleoresin formation in conifers in response to insect attack or other injury. Involved in diterpene (C20) olefins biosynthesis. Bifunctional enzyme that catalyzes two sequential cyclizations of geranylgeranyl diphosphate (GGPP) to abietadiene. The copalyl diphosphate (CPP) intermediate diffuses freely between the 2 active sites in the enzyme. Changes in reaction pH, but not salt concentration, influence the relative proportion of the major products of the enzyme, abitadiene, levopimaradiene and neoabitadiene.

7 Publications

Miscellaneous

The abietadiene synthase activity exhibits an absolute dependence on a divalent metal ion cofactor while the copalyl diphosphate synthase activity is not completely dependent.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Not inhibited by 13-cyclopropylidene or 16-methylidenegeranylgeranyl diphosphate. The copalyl diphosphate synthase activity is not susceptible to magnesium-dependent inhibition.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=3 µM for GGPP (in presence of magnesium)2 Publications
  2. KM=20 µM for GGPP (in absence of magnesium)2 Publications
  3. KM=0.4 µM for CPP (in presence of magnesium)2 Publications
  4. KM=10 µM for CPP (in absence of magnesium)2 Publications

pH dependencei

Optimum pH is 7.2 with GGPP as substrate and 8.7 with CPP as substrate.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: oleoresin biosynthesis

This protein is involved in the pathway oleoresin biosynthesis, which is part of Terpene metabolism.
View all proteins of this organism that are known to be involved in the pathway oleoresin biosynthesis and in Terpene metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei269SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi402Magnesium 4By similarity1
Metal bindingi404Magnesium 4By similarity1
Binding sitei489SubstrateBy similarity1
Metal bindingi621Magnesium 1By similarity1
Metal bindingi621Magnesium 2By similarity1
Metal bindingi625Magnesium 1By similarity1
Metal bindingi625Magnesium 2By similarity1
Metal bindingi765Magnesium 3By similarity1
Metal bindingi769Magnesium 3By similarity1
Metal bindingi773Magnesium 3By similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIsomerase, Lyase, Multifunctional enzyme
LigandMagnesium, Manganese, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.2.3.132, 2
4.2.3.18, 2

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00924

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Bifunctional abietadiene synthase, chloroplastic
Alternative name(s):
(-)-abieta-7(8),13(14)-diene synthase
Abietadiene cyclase
Short name:
AgAS
Agggabi
Including the following 2 domains:
Abietadiene synthase (EC:4.2.3.182 Publications)
Alternative name(s):
Neoabietadiene synthase (EC:4.2.3.1322 Publications)
Copalyl diphosphate synthase (EC:5.5.1.122 Publications)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:AS
Synonyms:ac22, ag22
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiAbies grandis (Grand fir) (Pinus grandis)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri46611 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinopsidaPinidaeConifers IPinalesPinaceaeAbies

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Chloroplast, Plastid

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi86K → A: No effect on CPP binding, but decreased abietadiene synthase activity; when associated with A-87. 1 Publication1
Mutagenesisi87R → A: No effect on CPP binding, but decreased abietadiene synthase activity; when associated with A-86. 1 Publication1
Mutagenesisi356R → A: No effect on abietadiene synthase activity, but strongly reduced copalyl diphosphate synthase activity. 1 Publication1
Mutagenesisi356R → H: Increased Mg(2+) inhibition; when associated with A-621. 1 Publication1
Mutagenesisi358W → A: Decreased copalyl diphosphate synthase activity. 1 Publication1
Mutagenesisi361D → A: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication1
Mutagenesisi365R → A: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication1
Mutagenesisi402D → A, E or N: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication1
Mutagenesisi404D → A, E or N: No effect on GGPP binding, but loss of copalyl diphosphate synthase activity. 2 Publications1
Mutagenesisi405D → A, E or N: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication1
Mutagenesisi411R → A: No effect on GGPP binding, but slightly decreased copalyl diphosphate synthase activity. 1 Publication1
Mutagenesisi451N → A: No effect on abietadiene synthase activity, but strongly reduced copalyl diphosphate synthase activity. 1 Publication1
Mutagenesisi454R → A: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication1
Mutagenesisi499E → A: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication1
Mutagenesisi520Y → A: No effect on GGPP binding, but slightly decreased copalyl diphosphate synthase activity. 1 Publication1
Mutagenesisi584R → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
Mutagenesisi586R → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
Mutagenesisi589E → A: Lower substrate binding and strong decrease of abietadiene synthase activity. 1 Publication1
Mutagenesisi617T → A: Increased production of abietadiene at the expense of levopimaradiene. 1 Publication1
Mutagenesisi621D → A: Loss of abietadiene synthase activity. Increased Mg(2+) inhibition; when associated with H-356. 3 Publications1
Mutagenesisi625D → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
Mutagenesisi699E → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
Mutagenesisi721S → A: Lower substrate binding and strong decrease of abietadiene synthase activity. 1 Publication1
Mutagenesisi723A → S: Produces pimaradienes instead of abietadienes. 1 Publication1
Mutagenesisi727V → T: No effect. 1 Publication1
Mutagenesisi762R → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
Mutagenesisi765N → A: Abolishes the conversion of CPP to abietadiene; produces only sandaracopimaradiene. 1 Publication1
Mutagenesisi766D → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
Mutagenesisi769T → A: Increased production of neoabietadiene at the expense of both levopimaradiene and abietadiene. 1 Publication1
Mutagenesisi773E → A: Increased production of neoabietadiene. 1 Publication1
Mutagenesisi778E → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
Mutagenesisi841Y → F: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
Mutagenesisi845D → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
Mutagenesisi848T → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 70ChloroplastSequence analysisAdd BLAST70
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003363471 – 868Bifunctional abietadiene synthase, chloroplasticAdd BLAST798

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The N-terminus is blocked.

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By wounding.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1868
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
Q38710

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q38710

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi402 – 405DXDD motifCurated4
Motifi621 – 625DDXXD motifCurated5

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic activity in the class II active site relevant for the cyclization of GGPP. The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity in the class I active site, presumably through binding to Mg2+.Curated

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the terpene synthase family. Tpsd subfamily.Curated

Keywords - Domaini

Transit peptide

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00684, Terpene_cyclase_plant_C1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.600.10, 1 hit
1.50.10.130, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008949, Isoprenoid_synthase_dom_sf
IPR044814, Terpene_cyclase_plant_C1
IPR001906, Terpene_synth_N
IPR036965, Terpene_synth_N_sf
IPR005630, Terpene_synthase_metal-bd
IPR008930, Terpenoid_cyclase/PrenylTrfase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01397, Terpene_synth, 1 hit
PF03936, Terpene_synth_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48239, SSF48239, 2 hits
SSF48576, SSF48576, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q38710-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAMPSSSLSS QIPTAAHHLT ANAQSIPHFS TTLNAGSSAS KRRSLYLRWG
60 70 80 90 100
KGSNKIIACV GEGGATSVPY QSAEKNDSLS SSTLVKREFP PGFWKDDLID
110 120 130 140 150
SLTSSHKVAA SDEKRIETLI SEIKNMFRCM GYGETNPSAY DTAWVARIPA
160 170 180 190 200
VDGSDNPHFP ETVEWILQNQ LKDGSWGEGF YFLAYDRILA TLACIITLTL
210 220 230 240 250
WRTGETQVQK GIEFFRTQAG KMEDEADSHR PSGFEIVFPA MLKEAKILGL
260 270 280 290 300
DLPYDLPFLK QIIEKREAKL KRIPTDVLYA LPTTLLYSLE GLQEIVDWQK
310 320 330 340 350
IMKLQSKDGS FLSSPASTAA VFMRTGNKKC LDFLNFVLKK FGNHVPCHYP
360 370 380 390 400
LDLFERLWAV DTVERLGIDR HFKEEIKEAL DYVYSHWDER GIGWARENPV
410 420 430 440 450
PDIDDTAMGL RILRLHGYNV SSDVLKTFRD ENGEFFCFLG QTQRGVTDML
460 470 480 490 500
NVNRCSHVSF PGETIMEEAK LCTERYLRNA LENVDAFDKW AFKKNIRGEV
510 520 530 540 550
EYALKYPWHK SMPRLEARSY IENYGPDDVW LGKTVYMMPY ISNEKYLELA
560 570 580 590 600
KLDFNKVQSI HQTELQDLRR WWKSSGFTDL NFTRERVTEI YFSPASFIFE
610 620 630 640 650
PEFSKCREVY TKTSNFTVIL DDLYDAHGSL DDLKLFTESV KRWDLSLVDQ
660 670 680 690 700
MPQQMKICFV GFYNTFNDIA KEGRERQGRD VLGYIQNVWK VQLEAYTKEA
710 720 730 740 750
EWSEAKYVPS FNEYIENASV SIALGTVVLI SALFTGEVLT DEVLSKIDRE
760 770 780 790 800
SRFLQLMGLT GRLVNDTKTY QAERGQGEVA SAIQCYMKDH PKISEEEALQ
810 820 830 840 850
HVYSVMENAL EELNREFVNN KIPDIYKRLV FETARIMQLF YMQGDGLTLS
860
HDMEIKEHVK NCLFQPVA
Length:868
Mass (Da):99,536
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iAD5E79F56B70D25C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti23A → T in AAK83563 (PubMed:11404343).Curated1
Sequence conflicti214F → S in AAK83563 (PubMed:11404343).Curated1
Sequence conflicti297 – 299DWQ → EWE in AAK83563 (PubMed:11404343).Curated3
Sequence conflicti557V → L in AAK83563 (PubMed:11404343).Curated1
Sequence conflicti579D → E in AAK83563 (PubMed:11404343).Curated1
Sequence conflicti653Q → K in AAK83563 (PubMed:11404343).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U50768 mRNA Translation: AAB05407.1
AF326516 Genomic DNA Translation: AAK83563.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:AAB05407

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50768 mRNA Translation: AAB05407.1
AF326516 Genomic DNA Translation: AAK83563.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3S9VX-ray2.30A/B/C/D85-868[»]
AlphaFoldDBiQ38710
SMRiQ38710
ModBaseiSearch...
PDBe-KBiSearch...

Genome annotation databases

KEGGiag:AAB05407

Enzyme and pathway databases

UniPathwayiUPA00924
BRENDAi4.2.3.132, 2
4.2.3.18, 2

Family and domain databases

CDDicd00684, Terpene_cyclase_plant_C1, 1 hit
Gene3Di1.10.600.10, 1 hit
1.50.10.130, 1 hit
InterProiView protein in InterPro
IPR008949, Isoprenoid_synthase_dom_sf
IPR044814, Terpene_cyclase_plant_C1
IPR001906, Terpene_synth_N
IPR036965, Terpene_synth_N_sf
IPR005630, Terpene_synthase_metal-bd
IPR008930, Terpenoid_cyclase/PrenylTrfase
PfamiView protein in Pfam
PF01397, Terpene_synth, 1 hit
PF03936, Terpene_synth_C, 1 hit
SUPFAMiSSF48239, SSF48239, 2 hits
SSF48576, SSF48576, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTPSDV_ABIGR
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q38710
Secondary accession number(s): Q94FW1
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: November 1, 1996
Last modified: May 25, 2022
This is version 112 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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